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Article
Nature Cell Biology  6, 207 - 214 (2004)
Published online: 22 February 2004; | doi:10.1038/ncb1099

Polypyrimidine tract-binding protein promotes insulin secretory granule biogenesis

Klaus-Peter Knoch1, Hendrik Bergert1, 2, Barbara Borgonovo1, Hans-Detlev Saeger2, Anke Altkrüger1, Paul Verkade3 & Michele Solimena1, 3

1  Experimental Diabetology, Carl Gustav Carus Medical School, University of Technology Dresden, Dresden 01307, Germany.

2  Department of Surgery, Carl Gustav Carus Medical School, University of Technology Dresden, Dresden 01307, Germany.

3  Max Planck Institute for Molecular Cell Biology and Genetics, Dresden 01307, Germany.

Correspondence should be addressed to Michele Solimena michele.solimena@mailbox.tu-dresden.de
Pancreatic beta-cells store insulin in secretory granules that undergo exocytosis upon glucose stimulation. Sustained stimulation depletes beta-cells of their granule pool, which must be quickly restored. However, the factors promoting rapid granule biogenesis are unknown. Here we show that beta-cell stimulation induces the nucleocytoplasmic translocation of polypyrimidine tract-binding protein (PTB). Activated cytosolic PTB binds and stabilizes mRNAs encoding proteins of secretory granules, thus increasing their translation, whereas knockdown of PTB expression by RNA interference (RNAi) results in the depletion of secretory granules. These findings may provide insight for the understanding and treatment of diabetes, in which insulin secretion is typically impaired.

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Nature Cell Biology
ISSN: 1465-7392
EISSN: 1476-4679
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